scholarly journals Unravelling the fibrillation mechanism of ovalbumin in the presence of mercury at its isoelectric pH

RSC Advances ◽  
2020 ◽  
Vol 10 (28) ◽  
pp. 16415-16421
Author(s):  
Manjumol Mathew ◽  
Charuvila T. Aravindakumar ◽  
Usha K. Aravind
Keyword(s):  
Mercuric Chloride ◽  
Nephila Clavipes ◽  
Isoelectric Ph

Mercuric chloride triggered ovalbumin aggregation pathway and its resemblance to Nephila clavipes.

scholarly journals ON THE ACTION OF MERCURIC CHLORIDE AND OF HYDROGEN DIOXIDE ON BILE PIGMENTS

1927 ◽  
Vol 72 (2) ◽  
pp. 635-641
Author(s):  
W.F. von Oettingen ◽  
Torald Sollmann
Keyword(s):  
Mercuric Chloride ◽  
Bile Pigments

Astrocytes as potential modulators of mercuric chloride neurotoxicity

1994 ◽  
Vol 14 (6) ◽  
pp. 637-652 ◽  
Author(s):  
M. Aschner ◽  
K. J. Mullaney ◽  
M. N. Fehm ◽  
D. E. Wagoner ◽  
D. Vitarella
Keyword(s):  
Mercuric Chloride

Inhibition of guanidinobenzoatase with mercuric chloride and m-iodobenzylguanidine

1986 ◽  
Vol 14 (5) ◽  
pp. 879-880
Author(s):  
FRANK S. STEVEN ◽  
MARGARET M. GRIFFIN ◽  
THERESIA L. H. WONG ◽  
RIFFAT YASMIN
Keyword(s):  
Mercuric Chloride

scholarly journals Nephila clavipes Flagelliform Silk-Like GGX Motifs Contribute to Extensibility and Spacer Motifs Contribute to Strength in Synthetic Spider Silk Fibers

2013 ◽  
Vol 14 (6) ◽  
pp. 1751-1760 ◽  
Author(s):  
Sherry L. Adrianos ◽  
Florence Teulé ◽  
Michael B. Hinman ◽  
Justin A. Jones ◽  
Warner S. Weber ◽  
...  
Keyword(s):  
Spider Silk ◽  
Nephila Clavipes ◽  
Silk Fibers

scholarly journals CAU-1, a Subclass B3 Metallo-β-Lactamase of Low Substrate Affinity Encoded by an Ortholog Present in the Caulobacter crescentus Chromosome

2002 ◽  
Vol 46 (6) ◽  
pp. 1823-1830 ◽  
Author(s):  
Jean-Denis Docquier ◽  
Fabrizio Pantanella ◽  
Francesco Giuliani ◽  
Maria Cristina Thaller ◽  
Gianfranco Amicosante ◽  
...  
Keyword(s):  
Caulobacter Crescentus ◽  
Hypothetical Protein ◽  
Exchange Chromatography ◽  
Substrate Affinity ◽  
Gene Encoding ◽  
Native Form ◽  
Significant Similarity ◽  
Expression Studies ◽  
Genes Encoding ◽  
Isoelectric Ph

ABSTRACT The sequenced chromosome of Caulobacter crescentus CB15 encodes a hypothetical protein that exhibits significant similarity (30 to 35% identical residues) to metallo-β-lactamases of subclass B3. An allelic variant of this gene (divergent by 3% of its nucleotides) was cloned in Escherichia coli from C. crescentus type strain DSM4727. Expression studies confirmed the metallo-β-lactamase activity of its product, CAU-1. The enzyme produced in E. coli was purified by two ion-exchange chromatography steps. CAU-1 contains a 29-kDa polypeptide with an alkaline isoelectric pH (>9), and unlike the L1 enzyme of Stenotrophomonas maltophilia, the native form is monomeric. Kinetic analysis revealed a preferential activity toward penicillins, carbapenems, and narrow-spectrum cephalosporins, while oxyimino cephalosporins were poorly or not hydrolyzed. Affinities for the various β-lactams were poor overall (Km values were always >100 μM and often >400 μM). The interaction with divalent ion chelators appeared to occur by a mechanism similar to that prevailing in other members of subclass B3. In C. crescentus, the CAU-1 enzyme is produced independently of β-lactam exposure and, interestingly, the bla CAU determinant is bracketed by three other genes, including two genes encoding enzymes involved in methionine biosynthesis and a gene encoding a putative transcriptional regulator, in an operon-like structure. The CAU-1 enzyme is the first example of a metallo-β-lactamase in a member of the α subdivision of the class Proteobacteria.

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